ID   FABP4_CEREL             Reviewed;         132 AA.
AC   A6YLM6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Fatty acid-binding protein, adipocyte;
DE   AltName: Full=Adipocyte-type fatty acid-binding protein;
DE            Short=A-FABP;
DE            Short=AFABP;
DE   AltName: Full=Fatty acid-binding protein 4;
GN   Name=FABP4;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone;
RA   Borsy A., Orosz L.;
RT   "Physiological versus pathological osteoporosis: Overlapping gene
RT   expression pattern in deer and human.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipid transport protein in adipocytes. Binds both long chain
CC       fatty acids and retinoic acid. Delivers long-chain fatty acids and
CC       retinoic acid to their cognate receptors in the nucleus.
CC       {ECO:0000250|UniProtKB:P04117}.
CC   -!- SUBUNIT: Monomer (By similarity). Homodimer. Interacts with PPARG (By
CC       similarity). {ECO:0000250|UniProtKB:P04117,
CC       ECO:0000250|UniProtKB:P15090}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus
CC       {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the
CC       ligand, a conformation change exposes a nuclear localization motif and
CC       the protein is transported into the nucleus. Subject to constitutive
CC       nuclear export. {ECO:0000250|UniProtKB:P04117}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC       ligand in its interior. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; EF619485; ABR68240.1; -; mRNA.
DR   AlphaFoldDB; A6YLM6; -.
DR   SMR; A6YLM6; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR   GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR033073; FABP4.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   PANTHER; PTHR11955:SF83; PTHR11955:SF83; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid-binding; Nucleus; Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P15090"
FT   CHAIN           2..132
FT                   /note="Fatty acid-binding protein, adipocyte"
FT                   /id="PRO_0000317431"
FT   MOTIF           22..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..129
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P15090"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04117"
FT   MOD_RES         20
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   132 AA;  14588 MW;  7A74D4EF5EB104F2 CRC64;
     MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPT LIISVNGDVV TIKSESTFKN
     TEISFKLGQE FDEVTPDDRK VKSTINLDGG ALVQVQNWDG KSTTIKRKLV DDKLVLECVM
     NGVTATRVYE RA